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Crystallization and preliminary characterization of three different crystal forms of human saposin C heterologously expressed in Pichia pastoris

Schultz-Heienbrok, Robert and Remmel, Natascha and Klingenstein, R. and Rossocha, Maksim and Sandhoff, Konrad and Saenger, Wolfram and Maier, Timm. (2006) Crystallization and preliminary characterization of three different crystal forms of human saposin C heterologously expressed in Pichia pastoris. Acta Crystallographica Section F, 62 (2). pp. 117-120.

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Abstract

The amphiphilic saposin proteins (A, B, C and D) act at the lipid–water interface in lysosomes, mediating the hydrolysis of membrane building blocks by water-soluble exohydrolases. Human saposin C activates glucocerebrosidase and β-­galactosylceramidase. The protein has been expressed in Pichia pastoris, purified and crystallized in three different crystal forms, diffracting to a maximum resolution of 2.5 Å. Hexagonal crystals grew from 2-propanol-containing solution and contain a single molecule in the asymmetric unit according to the Matthews coefficient. Orthorhombic and tetragonal crystals were both obtained with pentaerythritol ethoxylate and are predicted to contain two molecules in the asymmetric unit. Attempts to determine the respective crystal structures by molecular replacement using either the known NMR structure of human saposin C or a related crystal structure as search models have so far failed. The failure of the molecular-replacement method is attributed to conformational changes of the protein, which are known to be required for its biological activity. Crystal structures of human saposin C therefore might be the key to mapping out the conformational trajectory of saposin-like proteins.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Structural Biology & Biophysics > Structural Biology (Maier)
UniBasel Contributors:Maier, Timm
Item Type:Article, refereed
Article Subtype:Research Article
Publisher:Wiley
ISSN:1744-3091
e-ISSN:2053-230X
Note:Publication type according to Uni Basel Research Database: Journal article
Language:English
Identification Number:
Last Modified:18 Oct 2016 09:02
Deposited On:06 Oct 2016 11:27

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